Hostname: page-component-cd9895bd7-lnqnp Total loading time: 0 Render date: 2024-12-26T20:56:47.963Z Has data issue: false hasContentIssue false

Dissociation during dialysis of casein aggregates cross-linked by colloidal calcium phosphate in bovine casein micelles

Published online by Cambridge University Press:  01 June 2009

Takayoshi Aoki
Affiliation:
Department of Animal Science, Faculty of Agriculture, Kagoshima University, Kagoshima 890, Japan
Nagisa Yamada
Affiliation:
Department of Animal Science, Faculty of Agriculture, Kagoshima University, Kagoshima 890, Japan
Yoshitaka Kako
Affiliation:
Department of Animal Science, Faculty of Agriculture, Kagoshima University, Kagoshima 890, Japan
Tsuneaki Imamura
Affiliation:
Department of Applied Biochemistry, Faculty of Applied Biological Science, Hiroshima University, Fukuyama 720, Japan

Summary

Casein micelles separated by ultracentrifugation of raw skim milk were dispersed at a casein concentration of 2·5% in simulated milk ultrafiltrate and dialysed against 10 mM-imidazole buffer (pH 7·0) at 5 °C. The amounts of colloidal Ca and inorganic P decreased from 77 to 11 mg and from 31 to 2 mg respectively in 100 ml during 72 h of dialysis. Micellar casein content was reduced to 43 and 11% after 48 and 72 h of dialysis respectively. In high-performance gel chromatography of casein micelles in the presence of 6 M-urea, fraction 1, consisting of the casein aggregates cross-linked by colloidal Ca phosphate (CCP) decreased during dialysis and the retention time of the peak of fraction 1 was prolonged, suggesting that the cross-linkage between CCP and casein molecules was disrupted. The dissociation rates of the individual casein constituents from the casein aggregates cross-linked by CCP during dialysis were in the order β-> αs1 - > αs2-casein. The higher the ester phosphate content, the slower was the dissociation rate of the individual casein constituent. It is suggested that the strength of interaction between CCP and casein molecules depends on the ester phosphate content.

Type
Original articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1988

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Allen, R. J. L. 1940 The estimation of phosphorus. Biochemical Journal 34 858865Google Scholar
Aoki, T., Kako, Y. & Imamura, T. 1986 Separation of casein aggregates cross-linked by colloidal calcium phosphate from bovine casein micelles by high performance gel chromatography in the presence of urea. Journal of Dairy Research 53 5359Google Scholar
Aoki, T., Kawahara, A., Kako, Y. & Imamura, T. 1987 a Role of individual milk salt constituents in cross-linking by colloidal calcium phosphate in artificial casein micelles. Agricultural and Biological Chemistry 51 817821Google Scholar
Aoki, T., Yamada, N., Tomita, I., Kako, Y. & Imamura, T. 1987 b Caseins are cross-linked through their ester phosphate groups by colloidal calcium phosphate. Biochimica et Biophysica Acta 911 238243Google Scholar
Holt, C. 1985 The milk salts: their secretion, concentrations and physical chemistry. In Developments in Dairy Chemistry–3. Lactose and minor constituents pp. 143181 (Ed. Fox, P. F.) London: Elsevier Applied Science Publishers Ltd.Google Scholar
Holt, C., Davies, D. T. & Law, A. J. R. 1986 Effects of colloidal calcium phosphate content and free calcium ion concentration in the milk serum on the dissociation of bovine casein micelles. Journal of Dairy Research 53 557572CrossRefGoogle Scholar
Jenness, R. & Koops, J. 1962 Preparation and properties of a salt solution which simulates milk ultrnfiltrate. Netherlands Milk and Dairy Journal 16 153164Google Scholar
Lin, S. H. C., Leong, S. L., Dewan, R. K., Bloomfield, V. A. & Morr, C. V. 1972 Effect of calcium ion on the structure of native bovine casein micelles. Biochemistry 11 18181821Google Scholar
Morr, C. V., Josephson, R. V., Jenness, R. & Manning, P. B. 1971 Composition and properties of submicellar casein complexes in colloidal phosphate-free skimmilk. Journal of Dairy Science 54 15551563Google Scholar
Noble, R. W. & Waugh, D. F. 1965 Casein micelles. Formation and structure. I. Journal of the American Chemical Society 87 22362245Google Scholar
Ono, T., Dan, H. T. & Odagiri, S. 1978 Dissociation of bovine casein micelles by dialysis. Agricultural and Biological Chemistry 42 10631064Google Scholar
Ono, T., Furuyama, T. & Odagiri, S. 1981 Dissociation of large and small bovine casein micelles by dialysis. Agricultural and Biological Chemistry 45 511512Google Scholar
Ono, T., Hayakawa, Y. & Odagiri, S. 1975 The changes of the constituents of bovine casein micelles by calcium complexing agents. Journal of the Agricultural Chemical Society of Japan 50 99104Google Scholar
Pyne, G. T. 1962 Reviews of the progress of dairy science. Section C. Dairy Chemistry. Some aspects of the physical chemistry of the salts of milk. Journal of Dairy Research 29 101130Google Scholar
Rose, D. 1968 Relation between micellar and serum casein in bovine milk. Journal of Dairy Science 51 18971902Google Scholar
Schmidt, D. G. 1982 Association of caseins and casein micelle structure. In Developments in Dairy Chemistry-1. Proteins pp. 6186 (Ed. Fox, P. F.) London: Applied Science Publishers Ltd.Google Scholar
Schmidt, D. G. & Buchheim, W. 1970 [An electron-microscopic investigation of the substructure of the casein micelles in cow's milk.] Milchwissenschaft 25 596600Google Scholar
Swaisgood, H. E. 1982 Chemistry of milk protein. In Developments in Dairy Chemistry-1. Proteins pp. 159 (Ed. Fox, P. F.) London: Applied Science Publishers Ltd.Google Scholar